Two novel enzymes, NAD+-linked L-alloisocitrate (erythro-Ls-isocitrate) dehydrogenase and oxalosuccinate decarboxylase, were found and purified from a strain of Pseudomonas isolated as an L-alloisocitrate utilizing bacterium. The former enzyme catalyzes a reversible oxidation-reduction between L-alloisocitrate and oxalosuccinate which favors oxalosuccinate reduction. The latter enzyme catalyzes rapid decarboxylation of oxalosuccinate to α-ketoglutarate and CO2. Both enzymes require no metals for their activities. Complete oxidative decarboxylation of L-alloisocitrate to α-ketoglutarate occurs as a result of the sequential reactions catalyzed by these two enzymes. L-Alloisocitrate induces both enzymes in the growing pseudomonad.
|Number of pages||10|
|Journal||Journal of biochemistry|
|Publication status||Published - 1980 Jan 1|
ASJC Scopus subject areas
- Molecular Biology